Penentuan Tipe Inhibisi Senyawa Analog Kurkumin CA2 terhadap Enzim α-Glukosidase dari Beras Lapuk

Atiqoh Zummah; Endang  Astuti; Bambang Purwono

doi:10.29080/biotropic.v7i2.1952

Authors

Atiqoh Zummah Program Studi Biologi, Fakultas Sains dan Teknologi, Universitas Islam Negeri Sunan Ampel Surabaya, Surabaya, Indonesia
Endang Astuti Jurusan Kimia, Fakultas Matematika dan Ilmu Pengetahuan Alam, Universitas Gadjah Mada, Yogyakarta, Indonesia
Bambang Purwono Jurusan Kimia, Fakultas Matematika dan Ilmu Pengetahuan Alam, Universitas Gadjah Mada, Yogyakarta, Indonesia

DOI:

https://doi.org/10.29080/biotropic.v7i2.1952

Keywords:

inhibisi enzim, glukosidase, analog kurkumin

Abstract

Diabetes is a health problem that exists throughout the world, especially in Indonesia. Based on data compiled from the International Diabetes Federation (IDF) in 2017, people with diabetes in Indonesia reached 10.3 million people, and if not handled properly it is suspected that there will be an increase to 21.3 million people in 2030. Curcumin analog compounds can used for the treatment of diabetes by inhibiting the enzyme α-glucosidase. The curcumin analog compound used in this study was synthesized from 4 methoxybenzaldehyde with cyclopentanone which was then called the CA2 compound. The α-glucosidase enzyme used in this study was obtained through extraction of weathered rice with an optimum pH of 4.5 and the enzyme extract fraction used was fraction II which had the highest activity compared to fractions I and III. The results showed that the values of the kinetic parameters K_m and V_max of the extracted α-glucosidase enzyme were 1.53 mM and 0.03 U/mL, respectively. The K_m kinetic parameter value changed to 1.66 Mm while the V_max value did not change when the α-glucosidase enzyme was inhibited by CA2 compound, so that the type of inhibition shown by CA2 compound was competitive.

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References

Anonim. 1996. Enzymatic Assay of -Glucosidase (EC 3.2.1.20) p-Nitrophenyl -D-Glucosidase as Substrate Product Nos. G5003, G6136, G7256, G8889,

G0660, and G3651. Sigma quality control test procedure. Saint LouisMissouri.

Davidson, V.L. dan Sittman, D.B. 1999. Biochemistry, 4th edition. Lipincott Williams and Wilkins, Maryland.

Guariguata, L. 2012. By The Numbers: New Estimates From The IDF Diabetes Atlas Updatefor 2012. Diabetes Res. Clin. Pract. 98: 524–525.

Mishra, R., Chandra, R. 2016. Purification and Characterization of α-Glukosidase From Moss Hypophilla Nymaniana (Fleish) Musel. Asian Journal Pharmaceutical and Clinical Research. 9 (1): 179-186.

Papriani, N.P., et al. 2019. Purification and characterization of α-glucosidase

enzyme from rice groats. J. Phys.: Conf. Ser. 1341 032017.

Risma, D. 2012. Isolasi dan Karakterisasi Enzim -glukosidase Dari Beras Lapuk (Oryza sativa). Skripsi. Program Reguler Kimia, FMIPA UI, Depok.

Sharma, R.. 2012. Enzyme Inhibition: Mechanisms and Scope, Enzyme Inhibiton

and Bioapplications. InTech Web Publishers, Rijeka.

Shuler, M.L. and Kargi, F. 1992. Bioprocess Engineering Basic Concept. Prentice-Hall International Inc., New Jersey.

Whiting, D.R., Guariguata, L., Weil, C., and Shaw, J. 2011. IDF Diabetes Atlas: Global Estimates Ofthe Prevalence Of Diabetes For 2011 And 2030. Diabetes

Res. Clin. Pract. 94: 311–321.

Yuan, X., Li, H., Bai, H., Su, Z., Xiang, Q., Wang, C., Zhao, B., Zhang, Y., Zhang, Q., Chu, Y., and Huang, Y. 2014. Synthesis of Novel Curcumin Analogues For Inhibition Of 11-Hydroxysteroid Dehydrogenase Type 1 With Anti-Diabetic Properties. Eur. J. Med. Chem.. 77: 223-230.